Protein Summary

This protein contains two domains of similar fold (1-210+447-477, 251-446) linked by a helix containing a beta hairpin (213-446). Each domain adopts typical UDP N-acetylglucosamine acyltransferase like fold. This organization of acyltransferase domains is novel.

The sequence analysis using BLAST suggests that this protein contains a PaaY carbonic anhydrases acetyltransferase region (251-376). This region maps to the second domain of this protein. However, this domain lacks features such as insertions outside the triangle barrel. The first domain seems more feature-rich, and is structurally similar to part of N-acetylglucosamine-1-phosphate uridyltransferase (e.g. 1g97).

This protein is likely to dimerize through its C-terminal 447-477 region. There are only 4 full length homologous sequences, all of them are highly homologous to each other.

KEGG annotation of this protein seems to suggest that this protein is likely to involved in aminosugar metabolism and is likely multi-functional: UDP-N-acetylglucosamine pyrophosphorylase and glucosamine-1-phosphate N-acetyltransferase. The domain organization seems to support that.

In summary, it seems that this protein catalyzes the following reactions: